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[Preprint]. 2023 Jul 3:2023.07.03.547580. [Version 1] doi: 10.1101/2023.07.03.547580

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Figure 1. — (A) ATPase activity of myosin S1 constructs was measured over time with increasing actin concentrations. Data points were fitted using Michaelis Menten kinetics to obtain maximum ATPase activity (k_cat) and actin affinity (K_M). (B) Measured values of k_cat and K_M for HCM-linked β-MHC I467V and LVNC-linked β-MHC I467T S1 mutations. Neither mutation significantly altered maximal ATPase activity nor actin affinity. Data are represented as mean ± SEM. A one-way ANOVA was used to assess statistical significance (p<0.05) compared to β-MHC WT S1. N=6–11 curves per myosin S1 construct.